1w2l
From Proteopedia
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| - | [[Image:1w2l.gif|left|200px]]<br /><applet load="1w2l" size=" | + | [[Image:1w2l.gif|left|200px]]<br /><applet load="1w2l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w2l, resolution 1.30Å" /> | caption="1w2l, resolution 1.30Å" /> | ||
'''CYTOCHROME C DOMAIN OF CAA3 OXYGEN OXIDOREDUCTASE'''<br /> | '''CYTOCHROME C DOMAIN OF CAA3 OXYGEN OXIDOREDUCTASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W2L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus] with ACT, HEM and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] Known structural/functional Site: <scene name='pdbsite=AC1:Act Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1W2L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] Known structural/functional Site: <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:18:31 2008'' |
Revision as of 08:18, 3 February 2008
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CYTOCHROME C DOMAIN OF CAA3 OXYGEN OXIDOREDUCTASE
Overview
The cytochrome c domain of subunit II from the Rhodothermus marinus caa(3), HiPIP:oxygen oxidoreductase, a member of the superfamily of, heme-copper-containing terminal oxidases, was produced in Escherichia coli, and characterised. The recombinant protein, which shows the same optical, absorption and redox properties as the corresponding domain in the holo, enzyme, was crystallized and its structure was determined to a resolution, of 1.3 A by the multiwavelength anomalous dispersion (MAD) technique using, the anomalous dispersion of the heme iron atom. The model was refined to, final R(cryst) and R(free) values of 13.9% and 16.7%, respectively. The, structure reveals the insertion of two short antiparallel beta-strands, forming a small beta-sheet, an interesting variation of the classical all, alpha-helical cytochrome c fold. This modification appears to be common to, all known caa(3)-type terminal oxidases, as judged by comparative, modelling and by analyses of the available amino acid sequences for these, enzymes. This is the first high-resolution crystal structure reported for, a cytochrome c domain of a caa(3)-type terminal oxidase. The R.marinus, caa(3) uses HiPIP as the redox partner. The calculation of the, electrostatic potential at the molecular surface of this extra C-terminal, domain provides insights into the binding to its redox partner on one side, and its interaction with the remaining subunit II on the other side.
About this Structure
1W2L is a Single protein structure of sequence from Rhodothermus marinus with , and as ligands. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure at 1.3 A resolution of Rhodothermus marinus caa(3) cytochrome c domain., Srinivasan V, Rajendran C, Sousa FL, Melo AM, Saraiva LM, Pereira MM, Santana M, Teixeira M, Michel H, J Mol Biol. 2005 Feb 4;345(5):1047-57. Epub 2004 Dec 7. PMID:15644203
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